title: Rapamycin resistance: mTORC1 substrates hold some of the answers.
abstract: The mechanism of action of the mTOR inhibitor rapamycin is poorly understood and why certain mTORC1 phosphorylation sites are rapamycin insensitive remains elusive. Site-specific analysis of mTORC1 substrates now suggests that the sequence composition of a phosphorylation site determines whether it is sensitive to rapamycin and starvation.
authors.affiliation: Department of Cancer and Cell Biology, University of Cincinnati College of Medicine, Cincinnati, OH 45267, USA. Electronic address: yoonsh@ucmail.uc.edu.
authors.forename: Sang-Oh
authors.initials: SO
authors.lastname: Yoon
authors.forename: Philippe P
authors.initials: PP
authors.lastname: Roux
mesh_terms: D000818:Animals; D006801:Humans; D010455:Peptides / Q000378:metabolism*; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D020123:Sirolimus / Q000494:pharmacology*; D058570:TOR Serine-Threonine Kinases / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D010455:Peptides; D011506:Proteins; D058570:TOR Serine-Threonine Kinases; D020123:Sirolimus